1sa0: Difference between revisions

Revision as of 01:41, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sa0.png

Template:STRUCTURE 1sa0

TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEXTUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX

Template:ABSTRACT PUBMED 15014504

About this StructureAbout this Structure

1SA0 is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain., Ravelli RB, Gigant B, Curmi PA, Jourdain I, Lachkar S, Sobel A, Knossow M, Nature. 2004 Mar 11;428(6979):198-202. PMID:15014504

Page seeded by OCA on Tue Jul 29 01:41:25 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX'''
+===TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX===
-==Overview==
+<!--
-Microtubules are cytoskeletal polymers of tubulin involved in many cellular functions. Their dynamic instability is controlled by numerous compounds and proteins, including colchicine and stathmin family proteins. The way in which microtubule instability is regulated at the molecular level has remained elusive, mainly because of the lack of appropriate structural data. Here, we present the structure, at 3.5 A resolution, of tubulin in complex with colchicine and with the stathmin-like domain (SLD) of RB3. It shows the interaction of RB3-SLD with two tubulin heterodimers in a curved complex capped by the SLD amino-terminal domain, which prevents the incorporation of the complexed tubulin into microtubules. A comparison with the structure of tubulin in protofilaments shows changes in the subunits of tubulin as it switches from its straight conformation to a curved one. These changes correlate with the loss of lateral contacts and provide a rationale for the rapid microtubule depolymerization characteristic of dynamic instability. Moreover, the tubulin-colchicine complex sheds light on the mechanism of colchicine's activity: we show that colchicine binds at a location where it prevents curved tubulin from adopting a straight structure, which inhibits assembly.
+The line below this paragraph, {{ABSTRACT_PUBMED_15014504}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15014504 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15014504}}
 ==About this Structure==
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 [[Category: Stathmin]]
 [[Category: Tubulin]]
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